Purification and characterization of a protein antigen from Leptospira interrogans serovar hardjo, common to a wide range of bacteria.
A protein with a molecular mass of 64 kDa (P64) from Leptospira interrogans serovar hardjo was partially purified by using successively, phase partitioning with Triton X-114, ion-exchange chromatography and sucrose gradient centrifugation. Purification to homogeneity was obtained by electroelution of P64 from SDS-polyacrylamide gels. Monospecific rabbit antiserum (R alpha P64) was prepared using the purified protein preparation. P64 had a native molecular mass of greater than 670 kDa and was recognized by R alpha P64 as well as by human antisera. Western blotting of leptospiral serovars and 18 other bacterial species with R alpha P64 showed that P64 was cross-reactive with an equivalent antigen in a wide range of bacteria, indicating that it belongs to a family of antigens previously designated 'common antigen'. This putative common antigen from Leptospira appears to have a sub-surface location, but its function is not yet known.
Ballard
S A
SA
Department of Microbiology, Monash University, Melbourne, Victoria, Australia.
Faine
S
S
Adler
B
B
D000818:Animals; D000942:Antigens, Bacterial / Q000032:analysis*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002417:Cattle; D003429:Cross Reactions; D007921:Leptospira interrogans / Q000276:immunology*; D008970:Molecular Weight
D000942:Antigens, Bacterial; D001426:Bacterial Proteins